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Literature summary for 3.4.21.B30 extracted from

  • Fang, J.; Rand, K.D.; Silva, M.C.; Wales, T.E.; Engen, J.R.; Beuning, P.J.
    Conformational dynamics of the Escherichia coli DNA polymerase manager proteins UmuD and UmuD (2010), J. Mol. Biol., 398, 40-53.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B30

Protein Variants

Protein Variants Comment Organism
D3A the UmuD variant is non-cleavable but is a partial biological mimic of the cleaved form UmuD Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Subunits

Subunits Comment Organism
homodimer UmuD2 Escherichia coli

Synonyms

Synonyms Comment Organism
UmuD
-
 Escherichia coli
UmuD' UmuD is initially produced as a 139-amino-acid protein, which subsequently cleaves off its N-terminal 24 amino acids in a reaction dependent on RecA/single-stranded DNA, giving UmuD' Escherichia coli
UmuD2
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 UmuD2 and UmuD'2 each have a melting temperature of 60°C Escherichia coli

General Information

General Information Comment Organism
physiological function UmuD is implicated in a primitive DNA damage checkpoint and prevents DNA polymerase IV-dependent -1 frameshift mutagenesis, while the cleaved form UmuD' facilitates UmuC-dependent mutagenesis via formation of DNA polymerase V (UmuD'2C). Thus, the cleavage of UmuD is a crucial switch that regulates replication and mutagenesis via numerous protein-protein interactions. Escherichia coli